|Description||Green Fluorescent Protein|
|Overview||N-terminal HIS-tagged fusion protein corresponding to full-length Green Fluorescent Protein, expressed in E. coli.|
|Presentation||PBS containing 20% glycerol.|
|Entrez Gene Number|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||1 year at -20°C|
|Material Size||300 µg|
|Reference overview||Pub Med ID|
|Primary structure of the Aequorea victoria green-fluorescent protein. |
Prasher, D C, et al.
Gene, 111: 229-33 (1992) 1992
Many cnidarians utilize green-fluorescent proteins (GFPs) as energy-transfer acceptors in bioluminescence. GFPs fluoresce in vivo upon receiving energy from either a luciferase-oxyluciferin excited-state complex or a Ca(2+)-activated phosphoprotein. These highly fluorescent proteins are unique due to the chemical nature of their chromophore, which is comprised of modified amino acid (aa) residues within the polypeptide. This report describes the cloning and sequencing of both cDNA and genomic clones of GFP from the cnidarian, Aequorea victoria. The gfp10 cDNA encodes a 238-aa-residue polypeptide with a calculated Mr of 26,888. Comparison of A. victoria GFP genomic clones shows three different restriction enzyme patterns which suggests that at least three different genes are present in the A. victoria population at Friday Harbor, Washington. The gfp gene encoded by the lambda GFP2 genomic clone is comprised of at least three exons spread over 2.6 kb. The nucleotide sequences of the cDNA and the gene will aid in the elucidation of structure-function relationships in this unique class of proteins.